4G2R
Crystal Structure of the carboxyltransferase subunit of ACC (AccD6) in complex with inhibitor haloxyfop from Mycobacterium tuberculosis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| A | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0009274 | cellular_component | peptidoglycan-based cell wall |
| A | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016874 | molecular_function | ligase activity |
| A | 0019367 | biological_process | fatty acid elongation, saturated fatty acid |
| B | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| B | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0009274 | cellular_component | peptidoglycan-based cell wall |
| B | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016874 | molecular_function | ligase activity |
| B | 0019367 | biological_process | fatty acid elongation, saturated fatty acid |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE H1L A 501 |
| Chain | Residue |
| A | GLY98 |
| B | VAL337 |
| B | GLY341 |
| B | GLY366 |
| B | ALA370 |
| A | ALA99 |
| A | LEU108 |
| A | GLY137 |
| A | GLY138 |
| A | TYR141 |
| A | HOH940 |
| B | LEU295 |
| B | TYR326 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE H1L A 502 |
| Chain | Residue |
| A | VAL131 |
| A | ALA140 |
| A | PRO143 |
| A | VAL149 |
| A | MET151 |
| A | VAL157 |
| A | HIS184 |
| A | HIS185 |
| A | SER188 |
| A | HOH928 |
| B | GLN332 |
| B | GLU333 |
| B | TRP334 |
| B | GLY335 |
| B | VAL338 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE H1L B 501 |
| Chain | Residue |
| A | LEU295 |
| A | TYR326 |
| A | VAL337 |
| A | GLY341 |
| A | GLY366 |
| A | ALA370 |
| B | GLY98 |
| B | ALA99 |
| B | LEU108 |
| B | PHE115 |
| B | GLY137 |
| B | GLY138 |
| B | TYR141 |
| B | HOH777 |
| B | HOH857 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE H1L B 502 |
| Chain | Residue |
| A | GLN332 |
| A | GLU333 |
| A | TRP334 |
| A | VAL338 |
| B | VAL131 |
| B | ALA140 |
| B | PRO143 |
| B | VAL149 |
| B | MET151 |
| B | VAL157 |
| B | VAL159 |
| B | SER177 |
| B | HIS184 |
| B | HIS185 |
| B | SER188 |
| B | HOH941 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0007744|PDB:4G2R |
| Chain | Residue | Details |
| A | ALA99 | |
| A | GLY138 | |
| A | HIS185 | |
| A | TRP334 | |
| B | ALA99 | |
| B | GLY138 | |
| B | HIS185 | |
| B | TRP334 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609 |
| Chain | Residue | Details |
| A | THR2 | |
| B | THR2 |
